Engineered interaction between short elastin-like peptides and perfluorinated sulfonic-acid ionomer

Area of Science:

• Materials Science
• Electrochemistry
• Biotechnology

Background:

• Controlling ionomer thin films on metal surfaces is crucial for electrode performance in electrochemical applications.
• Engineered peptides offer tunable binding sites and structures for advanced electrode assembly.
• Simultaneous interaction of peptides with both ionomers and metals has not been previously demonstrated.

Purpose of the Study:

• To design a single-repeat elastin-like peptide capable of binding to both gold surfaces and perfluorinated sulfonic-acid ionomers (Nafion®).
• To investigate the ability of engineered peptides to mediate the formation of controlled ionomer layers on metal electrodes.
• To confirm peptide-ionomer interactions in solution and assess peptide structural integrity.

Main Methods:

• Quartz crystal microbalance with dissipation monitoring (QCM-D) to analyze peptide-ionomer layer formation on gold.
• Atomic force microscopy (AFM) for visualizing the ionomer layer morphology.
• Dynamic light scattering (DLS) to study peptide-ionomer interactions in solution.
• Circular dichroism (CD) spectroscopy to evaluate peptide secondary structure.

Main Results:

• A designed elastin-like peptide monolayer effectively attached to a gold surface.
• This peptide layer facilitated the formation of a thin, phase-separated ionomer film.
• Peptide-ionomer interactions were confirmed in solution, with peptides maintaining their secondary structures.
• The engineered peptide demonstrated dual binding capabilities to both gold and the ionomer.

Conclusions:

• Elastin-like peptides can be engineered for simultaneous binding to metals and ionomers.
• These engineered peptides serve as effective tools for controlling ionomer thin films on electrode surfaces.
• The findings highlight the potential of elastin-like peptides in advancing electrode engineering for electrochemical applications.